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By Monique M. Tirion, Daniel ben-Avraham, Kenneth C. Holmes (auth.), James E. Estes, Paul J. Higgins (eds.)

During the interval August 5-9, 1992, and instantly previous the 1992 Gordon learn convention on Motile and Contractile structures, the "Third overseas convention at the constitution and serve as of Ubiquitous mobile Protein Actin" used to be held on the Emma Willard university in Troy, long island, lower than the identify "ACTIN '92". This convention excited by the elemental homes and mobile features of actin and actin­ established microfilament platforms. the 1st convention during this sequence was once held in 1982, in Sydney, Australia, and hosted via Dr. Cristobal G. dos Remedios and Dr. Julian A. Barden, either from the collage of Sydney (New South Wales, Austrailia). the second one convention convened in Monza, Italy in June 1987, and was once equipped by means of Dr. Roberto Colombo, collage of Milan (Italy). This 3rd accumulating of researchers dedicated to the examine of actin and actin-associated proteins was once prepared by way of Dr. James E. Estes, Albany Stratton V A clinical middle and Dr. Paul 1. Higgins, Albany clinical university, who have been assisted by means of an Organizing Committee which includes Dr. Edward D. Korn (National middle, Lung and Blood Institute, NIH), Dr. Thomas P. Stossel (Massachusetts basic Hospital), Dr. Fumio Matsumura (Rutgers University), and Dr. Stephen Farmer (Boston University). This assembly used to be devoted to the various pioneering contributions of Professor Fumio Oosawa to the sphere of actin research.

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Additional resources for Actin: Biophysics, Biochemistry, and Cell Biology

Sample text

Estes. 1989. Preparation and polymerization properties of monomeric ADP-Actin. Biochem. Biophys. Acta 995:109-115. , LA. E. Estes. 1991. High Affmity Divalent Cation Exchange on Actin.

1969). This slow dehydration reaction limits the rate for association reactions of Mg+ + in its aquo-ion form (see Gershman et al, 1991, for more details). Thus the kinetics of the binding of Ca ++ to the high affinity site on actin are diffusion limited, but the kinetics of Mg+ + binding are limited by the characteristics of the Mg+ + aquo~ ion. The measured kinetics for binding of Ca ++ and Mg+ + to actin are consistent with the values for Kea and KMg reviewed in the previous section. 7 nM, in good agreement with the value of 1 nM from the more direct binding estimates.

1986), and if the starting Ca-actin were polymerized very slowly (but completely) in the presence of divalent cation concentrations [Ca] and [Mg], the proportion of Ca-actin incorporated in the polymer would also be fea . With faster polymerization of the initial Ca-actin, the proportion of Ca-actin incorporated in the polymer can only be greater than fea as polymerization competes with the Ca ++ / Mg ++ exchange reaction. 007 sec·1 which covers very slow to rapid polymerizations. The intercepts with the yaxis (at the left) reflect the slow polymerization limit (fea from Equation 3) for each [Ca]/[Mg] condition.

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